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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Deletion of the COOH terminus converts the ST5 p70 protein from an inhibitor of RAS signaling to an activator with transforming activity in NIH-3T3 cells.

Expression of the human protein ST5- p70 correlates with reduced tumorigenic phenotype in mammalian cells, reverts their transformed phenotype, and restores their contact-dependent growth. Furthermore, expression of p70 in COS-7 cells suppresses activation of mitogen activated protein kinase MAPK/ ERK2 by the largest ST5 product, p126, in response to epidermal growth factor stimulation. Here we show that deletions of the COOH-terminal region of p70 transform NIH3T3 cells and induce their anchorage-independent growth. Analysis of signaling leading to MAPK/ ERK2 stimulation revealed that in COS-7 cells, expression of either p70-DeltaC1 or p70-DeltaC2 markedly enhanced ERK2 activity in a growth factor-independent manner. Whereas wild-type p70 slightly inhibited ERK2 activation by RAS and MEK2, co-expression or p70-DeltaC1 or p70-DeltaC2 with either protein stimulated ERK2 cooperatively. This activity was completely blocked by the dominant negative mutants RAS17N or MEKAA, suggesting that p70 functions upstream of RAS. Unlike wild-type p70, expression of p70-DeltaC1 or p70-DeltaC2 mutant did not interfere with the ability of ST5-p126 to stimulate ERK2. Taken together, the data suggest that the COOH-terminal tail, residues 489-609, contains some of the critical determinants for the function of p70. Loss of this region converts the protein from an inhibitor to a constitutive activator of the RAS-ERK2 pathway.[1]

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